Schampera Janik N, Schwan Carsten
Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany.
Institute for Experimental and Clinical Pharmacology and Toxicology, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany.
Curr Opin Cell Biol. 2024 Dec;91:102442. doi: 10.1016/j.ceb.2024.102442. Epub 2024 Nov 6.
Septins are involved in many important cellular processes, and septin dysfunction has been implicated in various pathologies, such as cancer. Like other components of the cytoskeleton -F-actin, microtubules, and intermediate filaments-septins can self-assemble into filaments and higher-order structures. These non-polar filaments are assembled from complex and variable multimeric building blocks. Septins exhibit a distinct preference for interacting with actin and microtubule structures, particularly at the interface with cellular membrane. Although they are crucial for many vital cellular functions and are frequently observed at prominent cellular structures like stress fibers, cilia, and neuronal processes, our understanding of the regulation of septin filament dynamics and the organized assembly of higher-order structures remains limited. However, recent insights into the architecture of septin filaments, the structure of crucial septin domains, and their interactions with other cellular components (F-actin, microtubules, membranes) and regulatory proteins may now pave the way for rapid progress.
Septins参与许多重要的细胞过程,并且septin功能障碍与各种病理学有关,如癌症。与细胞骨架的其他成分——F-肌动蛋白、微管和中间丝一样,septins可以自我组装成细丝和更高阶的结构。这些非极性细丝由复杂且可变的多聚体构建块组装而成。Septins对与肌动蛋白和微管结构相互作用表现出明显的偏好,特别是在与细胞膜的界面处。尽管它们对许多重要的细胞功能至关重要,并且经常在诸如应力纤维、纤毛和神经元突起等突出的细胞结构中观察到,但我们对septin细丝动力学的调节以及高阶结构的有组织组装的理解仍然有限。然而,最近对septin细丝结构、关键septin结构域的结构及其与其他细胞成分(F-肌动蛋白、微管、膜)和调节蛋白相互作用的深入了解,现在可能为快速进展铺平道路。